Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases
Poly(ADP-ribosyl)ation is a post-translational modification of proteins that performs an essential regulatory function in the cellular response to DNA damage. The key enzyme synthesizing poly(ADP-ribose) (PAR) in the cells is poly(ADP-ribose) polymerase 1 (PARP1). Understanding the mechanisms of the...
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| Veröffentlicht in: | Biochemistry (Moscow) 2022, Vol.87 (Suppl 1), p.S32-S47 |
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| container_title | Biochemistry (Moscow) |
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| creator | Alemasova, Elizaveta E. Naumenko, Konstantin N. Sukhanova, Maria V. Lavrik, Olga I. |
| description | Poly(ADP-ribosyl)ation is a post-translational modification of proteins that performs an essential regulatory function in the cellular response to DNA damage. The key enzyme synthesizing poly(ADP-ribose) (PAR) in the cells is poly(ADP-ribose) polymerase 1 (PARP1). Understanding the mechanisms of the PARP1 activity regulation within the cells is necessary for development of the PARP1-targeted antitumor therapy. This review is devoted to the studies of the role of the RNA-binding protein YB-1 in the PARP1-catalyzed PARylation. The mechanisms of PARP1 activity stimulation by YB-1 protein can possibly be extended to other RNA-binding proteins involved in the maintenance of the genome stability. |
| doi_str_mv | 10.1134/S0006297922140048 |
| format | Article |
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The key enzyme synthesizing poly(ADP-ribose) (PAR) in the cells is poly(ADP-ribose) polymerase 1 (PARP1). Understanding the mechanisms of the PARP1 activity regulation within the cells is necessary for development of the PARP1-targeted antitumor therapy. This review is devoted to the studies of the role of the RNA-binding protein YB-1 in the PARP1-catalyzed PARylation. 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The key enzyme synthesizing poly(ADP-ribose) (PAR) in the cells is poly(ADP-ribose) polymerase 1 (PARP1). Understanding the mechanisms of the PARP1 activity regulation within the cells is necessary for development of the PARP1-targeted antitumor therapy. This review is devoted to the studies of the role of the RNA-binding protein YB-1 in the PARP1-catalyzed PARylation. The mechanisms of PARP1 activity stimulation by YB-1 protein can possibly be extended to other RNA-binding proteins involved in the maintenance of the genome stability.</description><subject>Adenosine diphosphate</subject><subject>ADP-ribosylation</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bioorganic Chemistry</subject><subject>Catalysis</subject><subject>DNA Damage</subject><subject>DNA repair</subject><subject>Enzymes</subject><subject>Genomes</subject><subject>Life Sciences</subject><subject>Metabolism</subject><subject>Microbiology</subject><subject>Nuclear factor I</subject><subject>Poly Adenosine Diphosphate Ribose</subject><subject>Poly ADP Ribosylation</subject><subject>Poly(ADP-ribose)</subject><subject>Poly(ADP-ribose) polymerase</subject><subject>Poly(ADP-ribose) Polymerases - metabolism</subject><subject>Post-translation</subject><subject>Proteins</subject><subject>Proteins - metabolism</subject><subject>Regulation</subject><subject>Review</subject><subject>Ribonucleic acid</subject><subject>Ribose</subject><subject>Ribosylation</subject><subject>RNA</subject><subject>RNA-binding protein</subject><issn>0006-2979</issn><issn>1608-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kE1Pg0AQhjdGY2v1B3gxJF7aAzo7uwvssdbPpIlN1YMXCR9LQwNsZeGAv16QqkmNp8nM-8w7k5eQUwoXlDJ--QQADkpXIlIOwL09MqQOeDYDDvtk2Ml2pw_IkTHrtkWQ7JAMmBBApSeG5G2pM2XpxHq9sqmVFtZSreosqFJddNOFzprx9HphL9NQm6YXJtYsqIKs-VCxFTY7jJp8DXJVBkaZY3KQBJlRJ9s6Ii-3N8-ze3v-ePcwm87tiCGvbC45TRh6oBLAKJQgaJx4yhWIEDqYuBhGFLngyIGpIATBqBPSOBYUE3QYG5Fx77sp9XutTOXnqYlUlgWF0rXx0RFtSNJxZYue76BrXZdF-11Ldf5cOh1FeyoqtTGlSvxNmeZB2fgU_C58_0_47c7Z1rkOcxX_bHyn3QLYA6aVipUqf0__7_oJsaCKDg</recordid><startdate>2022</startdate><enddate>2022</enddate><creator>Alemasova, Elizaveta E.</creator><creator>Naumenko, Konstantin N.</creator><creator>Sukhanova, Maria V.</creator><creator>Lavrik, Olga I.</creator><general>Pleiades Publishing</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>2022</creationdate><title>Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases</title><author>Alemasova, Elizaveta E. ; Naumenko, Konstantin N. ; Sukhanova, Maria V. ; Lavrik, Olga I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c324t-4941f3280ef02cb9051df8e75220b62f72bc124542403eab05316b1dd512f2633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Adenosine diphosphate</topic><topic>ADP-ribosylation</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Bioorganic Chemistry</topic><topic>Catalysis</topic><topic>DNA Damage</topic><topic>DNA repair</topic><topic>Enzymes</topic><topic>Genomes</topic><topic>Life Sciences</topic><topic>Metabolism</topic><topic>Microbiology</topic><topic>Nuclear factor I</topic><topic>Poly Adenosine Diphosphate Ribose</topic><topic>Poly ADP Ribosylation</topic><topic>Poly(ADP-ribose)</topic><topic>Poly(ADP-ribose) polymerase</topic><topic>Poly(ADP-ribose) Polymerases - metabolism</topic><topic>Post-translation</topic><topic>Proteins</topic><topic>Proteins - metabolism</topic><topic>Regulation</topic><topic>Review</topic><topic>Ribonucleic acid</topic><topic>Ribose</topic><topic>Ribosylation</topic><topic>RNA</topic><topic>RNA-binding protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alemasova, Elizaveta E.</creatorcontrib><creatorcontrib>Naumenko, Konstantin N.</creatorcontrib><creatorcontrib>Sukhanova, Maria V.</creatorcontrib><creatorcontrib>Lavrik, Olga I.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - 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The key enzyme synthesizing poly(ADP-ribose) (PAR) in the cells is poly(ADP-ribose) polymerase 1 (PARP1). Understanding the mechanisms of the PARP1 activity regulation within the cells is necessary for development of the PARP1-targeted antitumor therapy. This review is devoted to the studies of the role of the RNA-binding protein YB-1 in the PARP1-catalyzed PARylation. The mechanisms of PARP1 activity stimulation by YB-1 protein can possibly be extended to other RNA-binding proteins involved in the maintenance of the genome stability.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><pmid>35501985</pmid><doi>10.1134/S0006297922140048</doi></addata></record> |
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| ispartof | Biochemistry (Moscow), 2022, Vol.87 (Suppl 1), p.S32-S47 |
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| subjects | Adenosine diphosphate ADP-ribosylation Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Catalysis DNA Damage DNA repair Enzymes Genomes Life Sciences Metabolism Microbiology Nuclear factor I Poly Adenosine Diphosphate Ribose Poly ADP Ribosylation Poly(ADP-ribose) Poly(ADP-ribose) polymerase Poly(ADP-ribose) Polymerases - metabolism Post-translation Proteins Proteins - metabolism Regulation Review Ribonucleic acid Ribose Ribosylation RNA RNA-binding protein |
| title | Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases |
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